Analytical Data
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Gene name
POLR1D
- Application
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Alternative Names
AC19 DNA-directed RNA polymerase I subunit D RNA polymerase I 16KDA subunit
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y2S0
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Expression Region
1-133aa
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Molecular Weight
42.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
POLR1D, or RNA polymerase I subunit D, is a crucial component of the RNA polymerase I complex, which is responsible for synthesizing ribosomal RNA (rRNA) in eukaryotic cells. The ribosomal RNA is fundamental for ribosome biogenesis and, consequently, for protein synthesis, making POLR1D vital for cellular growth and proliferation. Research into the POLR1D recombinant protein has gained significant traction due to its potential implications in understanding various diseases, including cancer. Dysregulation of ribosome biogenesis is often associated with oncogenesis, and several studies have indicated that alterations in RNA polymerase activity can affect tumor growth and stability. Investigating the structure, function, and interactions of the POLR1D protein is essential for deciphering its role in both normal and pathological states. Recombinant POLR1D offers opportunities to study its biochemical properties and its interactions with other proteins within the ribosome synthesis pathway, thus providing insights into fundamental cellular mechanisms. This research not only contributes to our understanding of rRNA synthesis but also paves the way for potential therapeutic targets in diseases linked to ribosome biogenesis dysfunction. As the field progresses, elucidating the precise mechanisms and regulatory roles of POLR1D will be vital for advancing our knowledge of cell biology and developing novel interventions for related diseases.
